An ATF/CREB binding site is required for virus induction of the human interferon beta gene [corrected]

Du, Wei; Maniatis, Tom

doi:10.1073/pnas.89.6.2150

Cited by 105 publications

(62 citation statements)

References 34 publications

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“…However, simultaneous addition of a fixed amount of HMG I(Y) resulted in a significant increase in ATF-2 binding ( Fig. 9; (10,11,17,20,27), and ATF-2 binds to PRDIV (7). Binding sites for HMG I(Y) (8,34) are found in PRDII and PRDIV and are indicated.…”

Section: Methodsmentioning

confidence: 99%

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A striking similarity in the organization of the E-selectin and beta interferon gene promoters.

Whitley¹,

Thanos²,

Read³

et al. 1994

Mol. Cell. Biol.

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173

150

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Transcription of the endothelial leukocyte adhesion molecule 1 (E-selectin or ELAM-1) gene is induced by the inflammatory cytokines interleukin-1 beta and tumor necrosis factor alpha (TNF-alpha). In this report, we identify four positive regulatory domains (PDI to PDIV) in the E-selectin promoter that are required for maximal levels of TNF-alpha induction in endothelial cells. In vitro DNA binding studies reveal that two of the domains contain novel adjacent binding sites for the transcription factor NF-kappa B (PDIII and PDIV), a third corresponds to a recently described CRE/ATF site (PDII), and a fourth is a consensus NF-kappa B site (PDI). Mutations that decrease the binding of NF-kappa B to any one of the NF-kappa B binding sites in vitro abolished cytokine-induced E-selectin gene expression in vivo. Previous studies demonstrated a similar correlation between ATF binding to PDII and E-selectin gene expression. Here we show that the high-mobility-group protein I(Y) [HMG I(Y)] also binds specifically to the E-selectin promoter and thereby enhances the binding of both ATF-2 and NF-kappa B to the E-selectin promoter in vitro. Moreover, mutations that interfere with HMG I(Y) binding decrease the level of cytokine-induced E-selectin expression. The organization of the TNF-alpha-inducible element of the E-selectin promoter is remarkably similar to that of the virus-inducible promoter of the human beta interferon gene in that both promoters require NF-kappa B, ATF-2, and HMG I(Y). We propose that HMG I(Y) functions as a key architectural component in the assembly of inducible transcription activation complexes on both promoters.

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Section: Methodsmentioning

confidence: 99%

“…Transcriptional synergism between NF-KB and ATF-2 is also required for virus induction of the human beta interferon (IFN-1) gene (7). However, in this case the high-mobilitygroup protein I(Y) [HMG I(Y)] is required for the activity of both NF-KB (34) and ATF-2 (8).…”

mentioning

confidence: 99%

A striking similarity in the organization of the E-selectin and beta interferon gene promoters.

Whitley¹,

Thanos²,

Read³

et al. 1994

Mol. Cell. Biol.

Self Cite

173

150

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show abstract

“…The central DNA sequence of PRDIV contains an asymmetric ATF/CREB site, which upon virus induction is bound by a heterodimer of ATF-2 and c-jun (14,15,61). The core ATF-2-c-jun binding site, 5Ј-ATGACATAGG-3Ј, consists of a half-site (underlined) identical to that of the consensus CRE, 5Ј-ATGACGTCAT-3Ј (21), and a nonconsensus half-site.…”

Section: The Orientation Of An Asymmetric Atf-2-c-jun Site Is Requirementioning

confidence: 99%

Assembly of a Functional Beta Interferon Enhanceosome Is Dependent on ATF-2–c-jun Heterodimer Orientation

Falvo¹,

Parekh²,

Lin

et al. 2000

Molecular and Cellular Biology

124

112

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“…S1] (10)(11)(12). These transcription factors are activated and, therefore, type I IFN is induced by bacterial components, such as lipopolysaccharide, and CpG DNA in leukocytes, such as macrophages and dendritic cells, as well as by viral infection (13,14).…”

mentioning

confidence: 99%

Evolution of MDA-5/RIG-I-dependent innate immunity: Independent evolution by domain grafting

Sarkar

DeSalle

Fisher

2008

Proc. Natl. Acad. Sci. U.S.A.

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Interferons (IFNs) comprise a family of secreted proteins (cytokines) produced by cells following virus infection and create an antiviral state in neighboring cells (1-6). The relationship between IFN and viral infection is well documented and supported by studies employing neutralizing antibodies and IFN-receptor knockout mice, which document a direct role for IFN in mediating host defense against viruses (7,8). Moreover, IFNs are now recognized as multifunctional molecules that also provide defense against bacterial infection (especially intracellular parasites), induce antitumor activity (both direct and immune system-mediated), and stimulate or inhibit differentiation depending on cellular context (5, 9). In addition, type I IFNs also induce apoptosis of virus-infected cells and activate natural killer and T cells, thus activating the adaptive immune system as well (3).The expression of type I IFN is stringently regulated by the activation of pre-existing transcription factors, such as IFN regulatory factor 3 (IRF-3), NF-B, and ATF-2-c-Jun [supporting information (SI) Fig. S1] (10-12). These transcription factors are activated and, therefore, type I IFN is induced by bacterial components, such as lipopolysaccharide, and CpG DNA in leukocytes, such as macrophages and dendritic cells, as well as by viral infection (13,14). Targeted-gene-disruption studies indicate that Toll-like receptors (TLRs) recognize pathogenassociated molecular patterns. TLR3, TLR4, mouse TLR7 (human TLR8), and TLR9 function as signaling receptors for extracellular double-stranded RNA (dsRNA), lipopolysaccharide, viral single-stranded RNA, and CpG DNA, respectively (15-18). The interaction of these pathogen-associated molecular patterns with the extracellular leucine-rich repeat of the TLR facilitates the recruitment of adaptor molecules to the cytoplasmic Toll-IL-1 receptor domain of the TLR (19). The adaptors MyD88, IL-1 receptor associated kinase (IRAK), and TRAF6 are recruited by many TLRs and activate signaling cascades. For TLR7 and TLR9, type I IFN is induced by this MyD88-dependent pathway (19). TLR4 and TLR3 activate an additional signaling pathway called the MyD88-independent pathway, which recruits another adaptor molecule, Trif, and activates a second set of genes, including those of type I IFN, through activation of IRF-3 (20, 21). However, for most cell types, it has been postulated that the replication of viruses results in an accumulation of intracellular dsRNA, which triggers host response mechanisms that include expression of type I IFN (22). This signaling pathway is apparently distinct from that mediated by TLR3 and constitutes a major pathway activated by viral infection.Recent studies identified two proteins, melanoma differentiation associated gene-5 (MDA-5) and retinoic acid inducible gene I (RIG-I), as intracellular sensors of dsRNA responsible for induction of type I IFN (23, 24). Analysis of mda-5 or RIG-I knockout mice demonstrates that this TLR-independent pathway is central for innate immunity against viral ...

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An ATF/CREB binding site is required for virus induction of the human interferon beta gene [corrected]

Cited by 105 publications

References 34 publications

A striking similarity in the organization of the E-selectin and beta interferon gene promoters.

A striking similarity in the organization of the E-selectin and beta interferon gene promoters.

Assembly of a Functional Beta Interferon Enhanceosome Is Dependent on ATF-2–c-jun Heterodimer Orientation

Evolution of MDA-5/RIG-I-dependent innate immunity: Independent evolution by domain grafting

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